2kox: Difference between revisions
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<StructureSection load='2kox' size='340' side='right'caption='[[2kox]], [[NMR_Ensembles_of_Models | 640 NMR models]]' scene=''> | <StructureSection load='2kox' size='340' side='right'caption='[[2kox]], [[NMR_Ensembles_of_Models | 640 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2kox]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2kox]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KOX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KOX FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2k39|2k39]], [[1d3z|1d3z]], [[2nr2|2nr2]], [[1ubq|1ubq]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2k39|2k39]], [[1d3z|1d3z]], [[2nr2|2nr2]], [[1ubq|1ubq]]</div></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2kox FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kox OCA], [https://pdbe.org/2kox PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kox RCSB], [https://www.ebi.ac.uk/pdbsum/2kox PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kox ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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==See Also== | ==See Also== | ||
*[[ | *[[3D structures of ubiquitin|3D structures of ubiquitin]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 10:35, 2 February 2022
Structural highlights
Publication Abstract from PubMedLong-range correlated motions in proteins are candidate mechanisms for processes that require information transfer across protein structures, such as allostery and signal transduction. However, the observation of backbone correlations between distant residues has remained elusive, and only local correlations have been revealed using residual dipolar couplings measured by NMR spectroscopy. In this work, we experimentally identified and characterized collective motions spanning four beta-strands separated by up to 15 A in ubiquitin. The observed correlations link molecular recognition sites and result from concerted conformational changes that are in part mediated by the hydrogen-bonding network. Weak Long-Range Correlated Motions in a Surface Patch of Ubiquitin Involved in Molecular Recognition.,Fenwick RB, Esteban-Martin S, Richter B, Lee D, Walter KF, Milovanovic D, Becker S, Lakomek NA, Griesinger C, Salvatella X J Am Chem Soc. 2011 Jul 13;133(27):10336-10339. Epub 2011 Jun 20. PMID:21634390[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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